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Database: UniProt
Entry: A0A409XA56_PSICY
LinkDB: A0A409XA56_PSICY
Original site: A0A409XA56_PSICY 
ID   A0A409XA56_PSICY        Unreviewed;       510 AA.
AC   A0A409XA56;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Phosphoglycerate mutase-like protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CVT25_011445 {ECO:0000313|EMBL:PPQ87678.1};
OS   Psilocybe cyanescens.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Psilocybe.
OX   NCBI_TaxID=93625 {ECO:0000313|EMBL:PPQ87678.1, ECO:0000313|Proteomes:UP000283269};
RN   [1] {ECO:0000313|EMBL:PPQ87678.1, ECO:0000313|Proteomes:UP000283269}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2631 {ECO:0000313|EMBL:PPQ87678.1,
RC   ECO:0000313|Proteomes:UP000283269};
RX   PubMed=30283667; DOI=10.1002/evl3.42;
RA   Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA   Matheny P.B., Slot J.C.;
RT   "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT   diversity.";
RL   Evol. Lett. 2:88-101(2018).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000032};
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005375}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PPQ87678.1}.
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DR   EMBL; NHYD01002233; PPQ87678.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A409XA56; -.
DR   STRING; 93625.A0A409XA56; -.
DR   InParanoid; A0A409XA56; -.
DR   OrthoDB; 5486499at2759; -.
DR   Proteomes; UP000283269; Unassembled WGS sequence.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR11567:SF110; ACID PHOSPHATASE 1, ISOFORM B; 1.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 2.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000283269};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..510
FT                   /note="Phosphoglycerate mutase-like protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019162865"
SQ   SEQUENCE   510 AA;  57553 MW;  3300B82785389F33 CRC64;
     MRVRRGIKSR PFYFLLSCLI ALSFPHLIGA ENLVGDNHTC DNVLERTADC DPQRAAMTWN
     TTKEPTADFS AKMYGFRYPQ VPLEVDNYPV GPDTLQLEQV HVYVRHGERT PVGVRLKEAP
     ASIPEHWIMC RTARRFRAAV SSALGVGPNH IPHLSEVERE LDETLLTRRV VERKDGTLGE
     GECLLGELTD LGRHSTYIFG QNLRKLYVDR LGFIPDTLLS TNSVYFRSTN IPRTTESLQQ
     VIHGLYPTHK CHSTAQPPLL IRNGKDENLI GNTYACKRLE ILQVGFATAA AQAYNRSLER
     LDKKVSKYLN GNPIRVDGKP RASGVMDTIR AAIAHGIKVP PEFEDKNIVD VIVHKTEEVR
     RLAMGRLLDD MSRKMQSKVE RKESDPLKIL VHSTHDTAIA GLCSTFDVFD EKWPAFTASI
     TFELFKKREP EPDQARAQSI LSRMGSSSTS SQHYVRMRYQ NKDMVLPICA QDGDHLEGHP
     EFCTFSAFKA RVKELTPTEW DSECLPAGKP
//
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